at Google ScholarTitle data
Krammer, Carmen ; Suhre, Michael H. ; Kremmer, Elisabeth ; Diemer, Claudia ; Hess, Simone ; Schätzl, Hermann M. ; Scheibel, Thomas ; Vorberg, Ina M.:
Prion protein/protein interactions: fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells.
In: The FASEB Journal.
Vol. 22
(2008)
Issue 3
.
- pp. 762-773.
ISSN 0892-6638
DOI: https://doi.org/10.1096/fj.07-8733com
Abstract in another language
In mammalian prion diseases, an abnormally folded, aggregated form of the prion protein (PrPSc) appears to catalyze a conformational switch of its cellular isoform (PrPC) to an aggregated state. A similar prion-like phenomenon has been reported for the Saccharomyces cerevisiae translation termination factor Sup35p that can adopt a self-propagating conformation. We have compared aggregation propensities of chimeric proteins derived from the Sup35p prion domain NM and PrP in vitro and in the cytosol of mammalian cells. Sup35p-NM and PrP displayed strikingly different aggregation behaviors when expressed in mammalian cells, with NM remaining soluble and cytosolic PrP spontaneously aggregating due to the globular domain of PrP. When fused to PrP90–230, Sup35p-M exhibited an inhibitory effect for nucleation but increased aggregate growth, potentially by facilitating recruitment of newly synthesized chimeric proteins into the growing aggregates. This effect, however, could, to some extent, be counteracted by the prion-forming region Sup35p-N, thereby increasing aggregate frequency. Interestingly, a lowered nucleation rate was also observed in the presence of the amino-terminal region of PrP, suggesting that Sup35p-M and PrP23–90 share some biological function in prion protein assembly. Our results provide new insights into prion protein aggregation behaviors, demonstrating the impact of dynamic interactions between prion domains and suggesting that aggregation of yeast and mammalian prion proteins is strongly influenced by yet unidentified cellular conditions or factors.—Krammer C., Suhre, M. H., Kremmer, E., Diemer, C., Hess, S., Schätzl, H. M., Scheibel, T., Vorberg, I. Prion protein/protein interactions: fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells
Further data
| Item Type: | Article in a journal |
|---|---|
| Refereed: | Yes |
| Institutions of the University: | Faculties Faculties > Faculty of Engineering Science Faculties > Faculty of Engineering Science > Chair Biomaterials Faculties > Faculty of Engineering Science > Chair Biomaterials > Chair Biomaterials - Univ.-Prof. Dr. Thomas Scheibel Profile Fields > Advanced Fields > Advanced Materials Profile Fields > Advanced Fields > Molecular Biosciences Profile Fields > Advanced Fields > Polymer and Colloid Science Profile Fields > Emerging Fields > Food and Health Sciences Profile Fields Profile Fields > Advanced Fields Profile Fields > Emerging Fields |
| Result of work at the UBT: | Yes |
| DDC Subjects: | 600 Technology, medicine, applied sciences 600 Technology, medicine, applied sciences > 620 Engineering |
| Date Deposited: | 24 Sep 2015 07:29 |
| Last Modified: | 26 Nov 2015 10:51 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/19523 |